PLCG2

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An Error has occurred retrieving Wikidata item for infobox 1-Phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-2 is an enzyme that in humans is encoded by the PLCG2 gene.[1][2]

Function

From OMIM as of March 24, 2020:[3]

Enzymes of the phospholipase C family catalyze the hydrolysis of phospholipids to yield diacylglycerols and water-soluble phosphorylated derivatives of the lipid head groups. A number of these enzymes have specificity for phosphoinositides. Of the phosphoinositide-specific phospholipase C enzymes, C-beta is regulated by heterotrimeric G protein-coupled receptors, while the closely related C-gamma-1 (PLCG1; MIM 172420) and C-gamma-2 enzymes are controlled by receptor tyrosine kinases. The C-gamma-1 and C-gamma-2 enzymes are composed of phospholipase domains that flank regions of homology to noncatalytic domains of the SRC oncogene product, SH2 and SH3.

Interactions

PLCG2 has been shown to interact with:

References

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  1. ^ Page Module:Citation/CS1/styles.css has no content.Hernandez D, Egan SE, Yulug IG, Fisher EM (February 1995). "Mapping the gene that encodes phosphatidylinositol-specific phospholipase C-gamma 2 in the human and the mouse". Genomics. 23 (2): 504–7. doi:10.1006/geno.1994.1533. PMID 7835906.
  2. ^ Page Module:Citation/CS1/styles.css has no content."Entrez Gene: PLCG2 phospholipase C, gamma 2 (phosphatidylinositol-specific)".
  3. ^ Page Module:Citation/CS1/styles.css has no content.Bocchini CA (March 24, 2020). "600220: PHOSPHOLIPASE C, GAMMA-2; PLCG2". OMIM. Johns Hopkins University. Retrieved January 29, 2023.
  4. ^ a b Page Module:Citation/CS1/styles.css has no content.Guo B, Kato RM, Garcia-Lloret M, Wahl MI, Rawlings DJ (August 2000). "Engagement of the human pre-B cell receptor generates a lipid raft-dependent calcium signaling complex". Immunity. 13 (2): 243–53. doi:10.1016/s1074-7613(00)00024-8. PMID 10981967.
  5. ^ Page Module:Citation/CS1/styles.css has no content.Yasuda T, Tezuka T, Maeda A, Inazu T, Yamanashi Y, Gu H, Kurosaki T, Yamamoto T (July 2002). "Cbl-b positively regulates Btk-mediated activation of phospholipase C-gamma2 in B cells". J. Exp. Med. 196 (1): 51–63. doi:10.1084/jem.20020068. PMC 2194016. PMID 12093870.
  6. ^ a b c Page Module:Citation/CS1/styles.css has no content.Boudot C, Kadri Z, Petitfrère E, Lambert E, Chrétien S, Mayeux P, Haye B, Billat C (October 2002). "Phosphatidylinositol 3-kinase regulates glycosylphosphatidylinositol hydrolysis through PLC-gamma(2) activation in erythropoietin-stimulated cells". Cell. Signal. 14 (10): 869–78. doi:10.1016/s0898-6568(02)00036-0. PMID 12135708.
  7. ^ Page Module:Citation/CS1/styles.css has no content.Pleiman CM, Clark MR, Gauen LK, Winitz S, Coggeshall KM, Johnson GL, Shaw AS, Cambier JC (September 1993). "Mapping of sites on the Src family protein tyrosine kinases p55blk, p59fyn, and p56lyn which interact with the effector molecules phospholipase C-gamma 2, microtubule-associated protein kinase, GTPase-activating protein, and phosphatidylinositol 3-kinase". Mol. Cell. Biol. 13 (9): 5877–87. doi:10.1128/MCB.13.9.5877. PMC 360336. PMID 8395016.
  8. ^ Page Module:Citation/CS1/styles.css has no content.Perskvist N, Zheng L, Stendahl O (January 2000). "Activation of human neutrophils by Mycobacterium tuberculosis H37Ra involves phospholipase C gamma 2, Shc adapter protein, and p38 mitogen-activated protein kinase". J. Immunol. 164 (2): 959–65. doi:10.4049/jimmunol.164.2.959. PMID 10623845. S2CID 19134463.

Further reading

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